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Journal of Plant Biology

, Volume 48, Issue 4, pp 422–428 | Cite as

Biochemical characterization of anArabidopsis glucosyltransferase with high activity toward Jasmonic acid

  • Jong Tae Song
Article

Abstract

Biochemical characterization of the recombinant gene products from theArabidopsis glucosyltransferase multigene family has identified one enzyme with high activity toward the plant cellular regulator jasmonic acid (JA). The protein, AtJGT1 (UDP-glucose:JA glucosyltransferase), also has significant activities with other substrates, such as dihydrojasmonicacid, indole-3-acetic acid (IAA), indole-3-propionic acid, and indole-3-butyric acid. TheK M values of AtJGT1 for JA or IAA are similar to those of anArabidopsis IAA glucosyltransferase UGT84B1 previously reported. Northern blot analysis showed thatAtJGTI is highly expressed in the leaves, but only slightly detectable in the roots, stems, and inflorescences. This study describes the first biochemical analysis of a recombinant glucosyltransferase with JA activity, and provides the foundation for future genetic approaches to understanding the role of JA-glucose inArabidopsis.

Keywords

glucosyltransferase hormone homeostasis indole-3-acetic acid jasmonic acid JA conjugate 

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Copyright information

© The Botanical Society of Korea 2005

Authors and Affiliations

  1. 1.Division of Plant BiosciencesKyungpook National UniversityDaeguKorea

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